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Wyszukujesz frazę "Wang, Yi" wg kryterium: Autor


Wyświetlanie 1-3 z 3
Tytuł:
Non-histone nuclear protein HMGN2 differently regulates the urothelium barrier function by altering expression of antimicrobial peptides and tight junction protein genes in UPEC J96-infected bladder epithelial cell monolayer
Autorzy:
Tian, Hanwen
Miao, Junming
Zhang, Fumei
Xiong, Feng
Zhu, Feimei
Li, Jinyu
Wang, Xiaoying
Chen, Shanzhe
Chen, Junli
Huang, Ning
Wang, Yi
Powiązania:
https://bibliotekanauki.pl/articles/1038529.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
HMGN2
UPEC
BECs 5637
bladder epithelium
tight junction
antimicrobial peptides
Opis:
The urinary tract is vulnerable to frequent challenges from environmental microflora. Uropathogenic Escherichia coli (UPEC) makes a major contribution to urinary tract infection (UTI). Previous studies have characterized positive roles of non-histone nuclear protein HMGN2 in lung epithelial innate immune response. In the study presented here, we found HMGN2 expression was up-regulated in UPEC J96-infected urothelium. Surprisingly, over-expression of HMGN2 promoted disruption of BECs 5637 cells' intercellular junctions by down-regulating tight junction (TJs) components' expression and physical structure under J96 infection. Further investigation showed that BECs 5637 monolayer, in which HMGN2 was over-expressed, had significantly increased permeability to J96. Our study systemically explored the regulatory roles of HMGN2 in BECs barrier function during UPEC infection and suggested different modulations of intracellular and paracellular routes through which UPEC invades the bladder epithelium.
Źródło:
Acta Biochimica Polonica; 2018, 65, 1; 93-100
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Biochemical characterization of a catalase from Vibrio vulnificus, a pathogen that causes gastroenteritis
Autorzy:
Pei, Jihua
Wang, Haijun
Wu, Limin
Xia, Shenglong
Xu, Changlong
Zheng, Bo
Li, Tianya
Jiang, Yi
Powiązania:
https://bibliotekanauki.pl/articles/1038620.pdf
Data publikacji:
2017
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
catalase
Vibrio vulnificus
kinetics
mutation
gastroenteritis.
Opis:
Vibrio vulnificus is a virulent human pathogen causing gastroenteritis and possibly life threatening septicemia in patients. Most V. vulnificus are catalase positive and can deactivate peroxides, thus allowing them to survive within the host. In the study presented here, a catalase from V. vulnificus (CAT-Vv) was purified to homogeneity after expression in Escherichia coli. The kinetics and function of CAT-Vv were examined. CAT-Vv catalyzed the reduction of H2O2 at an optimal pH of 7.5 and temperature of 35°C. The Vmax and Km values were 65.8±1.2 U/mg and 10.5±0.7 mM for H2O2, respectively. Mutational analysis suggests that amino acids involved in heme binding play a key role in the catalysis. Quantitative reverse transcription-PCR revealed that in V. vulnificus, transcription of CAT-Vv was upregulated by low salinity, heat, and oxidative stresses. This research gives new clues to help inhibit the growth of, and infection by V. vulnificus.
Źródło:
Acta Biochimica Polonica; 2017, 64, 3; 543-549
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.
Autorzy:
Zhang, Jiayi
Dai, Jianliang
Zhao, Enpeng
Lin, Yun
Zeng, Li
Chen, Jinzhong
Zheng, Huari
Wang, Yu
Li, Xin
Ying, Kang
Xie, Yi
Mao, YuMin
Powiązania:
https://bibliotekanauki.pl/articles/1041522.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ovary
ePAD
peptidylarginine deiminase
hPADVI
Opis:
Peptidylarginine deiminase (PAD) catalyzes the post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Human, similar to rodents, has four isoforms of PAD (type I, II, III and IV/V), each of which is distinct in substrate specificity and tissue specific expression. In our large-scale sequencing project, we identified a new human PAD cDNA from a human fetal brain cDNA library. The putative protein encoded by this cDNA is designated hPADVI. Expression analysis of hPADVI showed that it is mainly expressed in adult human ovary and peripheral blood leukocytes. We conclude that hPADVI may be orthologous to mouse ePAD, basing on sequence comparison, chromosome localization and exon-intron structure analysis. PAD-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development. This study describes a new important member of the human PAD family.
Źródło:
Acta Biochimica Polonica; 2004, 51, 4; 1051-1058
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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